Please use this identifier to cite or link to this item:
https://hdl.handle.net/2440/134997
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Type: | Journal article |
Title: | Insights into the Interaction between Immobilized Biocatalysts and Metal–Organic Frameworks: A Case Study of PCN-333 |
Author: | Yang, W. Liang, W. O’Dell, L.A. Toop, H.D. Maddigan, N. Zhang, X. Kochubei, A. Doonan, C.J. Jiang, Y. Huang, J. |
Citation: | JACS Au, 2021; 1(12):2172-2181 |
Publisher: | American Chemical Society (ACS) |
Issue Date: | 2021 |
ISSN: | 2691-3704 2691-3704 |
Statement of Responsibility: | Wenjie Yang, Weibin Liang, Luke A. O, Dell, Hamish D. Toop, Natasha Maddigan, Xingmo Zhang, Alena Kochubei, Christian J. Doonan, Yijiao Jiang, and Jun Huang |
Abstract: | The immobilization of enzymes in metal−organic frameworks (MOFs) with preserved biofunctionality paves a promising way to solve problems regarding the stability and reusability of enzymes. However, the rational design of MOF-based biocomposites remains a considerable challenge as very little is known about the state of the enzyme, the MOF support, and their host−guest interactions upon immobilization. In this study, we elucidate the detailed host−guest interaction for MOF immobilized enzymes in the biointerface. Two enzymes with different sizes, lipase and insulin, have been immobilized in a mesoporous PCN333(Al) MOF. The dynamic changes of local structures of the MOF host and enzyme guests have been experimentally revealed for the existence of the confinement effect to enzymes and van der Waals interaction in the biointerface between the aluminum oxo-cluster of the PCN-333 and the -NH2 species of enzymes. This kind of host−guest interaction renders the immobilization of enzymes in PCN-333 with high affinity and highly preserved enzymatic bioactivity. |
Keywords: | metal−organic frameworks; enzyme immobilization; solid-state NMR; biointerface interaction; biocatalysis |
Rights: | © 2021 The Authors. Published by American Chemical Society. Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0) |
DOI: | 10.1021/jacsau.1c00226 |
Grant ID: | http://purl.org/au-research/grants/arc/DP180104010 http://purl.org/au-research/grants/arc/DP170103531 http://purl.org/au-research/grants/arc/DP200102411 |
Published version: | http://dx.doi.org/10.1021/jacsau.1c00226 |
Appears in Collections: | Physics publications |
Files in This Item:
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hdl_134997.pdf | Published version | 2.91 MB | Adobe PDF | View/Open |
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